CD47 (E2V9V) Rabbit mAb #36096
- WB
- IHC
Supporting Data
| REACTIVITY | M |
| SENSITIVITY | Endogenous |
| MW (kDa) | 45-50 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- M-Mouse
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunohistochemistry (Paraffin) | 1:50 - 1:200 |
Storage
For a carrier free (BSA and azide free) version of this product see product #83528.
Protocol
Specificity / Sensitivity
CD47 (E2V9V) Rabbit mAb recognizes endogenous levels of total CD47 protein.
Species Reactivity:
Mouse
Source / Purification
Monoclonal antibody is produced by immunizing animals with mouse CD47 recombinant protein.
Background
CD47 is a five-pass transmembrane protein expressed on all normal cells. It binds to the SIRPα that is expressed on myeloid cells, including macrophages, and neuronal cells in the central nervous system. Binding of CD47 to SIRPα promotes phosphorylation of tyrosine residues in the immunoreceptor tyrosine-based inhibitory motifs (ITIMs) within the SIRPα cytoplasmic tail, inhibiting macrophage phagocytosis toward CD47-expressing cells. In this way, CD47 serves as a "don't eat me" signal or a marker of "self", functioning as an innate immune checkpoint. Additionally, CD47 was reported to modulate lymphocyte cell activation and proliferation (1-3). CD47 is overexpressed in many types of cancer. The expression level of CD47 on cancer cells is negatively associated with the response to therapies, and low expression on tumor cells is associated with a better prognosis and survival. Reagents that can block CD47-SIRPα interaction are being actively pursued for therapeutic applications (4,5). In addition to SIRPα, other proteins have been reported to bind to CD47. Thrombospondin-1 (TSP1) competes with SIRPα to bind to CD47 in the extracellular region and activates signaling pathways downstream of CD47 (6). CD47 can laterally associate with VEGFR2, FAS, and certain integrins in different contexts, and influences their downstream signaling (7-9). CD47 can be shed from the cell surface by proteolytic cleavage. In addition, CD47 is present on extracellular vesicles including exosomes, suggesting additional extracellular signaling potential (10).
- Murata, Y. et al. (2014) J Biochem 155, 335-44.
- Legrand, N. et al. (2011) Proc Natl Acad Sci USA 108, 13224-9.
- Barclay, A.N. and Van den Berg, T.K. (2014) Annu Rev Immunol 32, 25-50.
- Weiskopf, K. (2017) Eur J Cancer 76, 100-109.
- Matlung, H.L. et al. (2017) Immunol Rev 276, 145-164.
- Roberts, D.D. et al. (2012) Matrix Biol 31, 162-9.
- Kaur, S. et al. (2010) J Biol Chem 285, 38923-32.
- Azcutia, V. et al. (2013) Mol Biol Cell 24, 3358-68.
- Quesada, A.J. et al. (2005) Cell Death Differ 12, 649-58.
- Soto-Pantoja, D.R. et al. (2015) Crit Rev Biochem Mol Biol 50, 212-30.
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